ID   VEGFA_CAVPO             Reviewed;         164 AA.
AC   P26617;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Vascular endothelial growth factor A;
DE            Short=VEGF-A;
DE   AltName: Full=Vascular permeability factor;
DE            Short=VPF;
GN   Name=VEGFA; Synonyms=VEGF;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bile duct;
RA   Berse B.;
RL   Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Growth factor active in angiogenesis, vasculogenesis and
CC       endothelial cell growth. Induces endothelial cell proliferation,
CC       promotes cell migration, inhibits apoptosis and induces
CC       permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and
CC       KDR/VEGFR2 receptors, heparan sulfate and heparin (By similarity).
CC       Binding to NRP1 receptor initiates a signaling pathway needed for motor
CC       neuron axon guidance and cell body migration, including for the caudal
CC       migration of facial motor neurons from rhombomere 4 to rhombomere 6
CC       during embryonic development (By similarity). Also binds the
CC       DEAR/FBXW7-AS1 receptor (By similarity). {ECO:0000250|UniProtKB:P15692,
CC       ECO:0000250|UniProtKB:Q00731}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Also found as
CC       heterodimer with PGF (By similarity). Interacts with NRP1 (By
CC       similarity). Interacts with BSG (By similarity).
CC       {ECO:0000250|UniProtKB:P15692, ECO:0000250|UniProtKB:P16612}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted but remains
CC       associated to cells or to the extracellular matrix unless released by
CC       heparin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M84230; AAA37057.1; -; mRNA.
DR   PIR; A60706; A60706.
DR   AlphaFoldDB; P26617; -.
DR   SMR; P26617; -.
DR   InParanoid; P26617; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR   CDD; cd00135; PDGF; 1.
DR   Gene3D; 2.10.160.10; -; 1.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR023581; PD_growth_factor_CS.
DR   InterPro; IPR000072; PDGF/VEGF_dom.
DR   InterPro; IPR027928; VEGF_C.
DR   InterPro; IPR036841; VEGF_C_sf.
DR   Pfam; PF00341; PDGF; 1.
DR   Pfam; PF14554; VEGF_C; 1.
DR   SMART; SM00141; PDGF; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   SUPFAM; SSF57593; SSF57593; 1.
DR   PROSITE; PS00249; PDGF_1; 1.
DR   PROSITE; PS50278; PDGF_2; 1.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted.
FT   CHAIN           1..164
FT                   /note="Vascular endothelial growth factor A"
FT                   /id="PRO_0000162361"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        25..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        50
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        59
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..103
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   164 AA;  19330 MW;  9EB86A81A9D5DCA4 CRC64;
     APMAEGEQKP REEVKFMDVY KRSYCRPIEM LVDIFQEYPD EIEYIFKPSC VPLMRCGGCC
     NDESLECVPT EEFNITMQIM RIKPHQGQHI GEMSFLQHSK CECRPKKEKA RQENPCGPCS
     ERRKHLFVQD PQTCKCSCRN TDSRCKARQL ELNERTCRCD KPRR